Nuclear magnetic resonance relaxation measurements are to be made on water resonances, and solute resonances in systems containing significant concentrations of the water-protein or water macromolecule interface in order to understand the structure and dynamics of this interfacial region. Three populations of water have been distinguished within lysozyme protein crystals, one of which is usual water in that it freezes. The enthalpy of fusion of this population will be measured using scanning calorimetry and nmr signal intensity measurements. The nature of the water molecule motions on the macromolecule surface will be studied further by the investigation of the temperature dependence of the nmr relaxation rates as a function of water content of the samples. The deuterium nuclear magnetic resonance relaxation parameters will be studied in protein systems to determine further the time scale of the water molecule reorientation. Electron spin resonance methods will be used to investigate the nature of protein side chain motions as a function of the water concentration in protein powders and the nature of apparent phase transition observed in the dynamic parameters associated with this low solvent systems. Solute resonances, lithium, sodium, and fluorine will be investigated within protein crystals to determine the dynamics of their motion and modes of relaxation. The theory of the nuclear relaxation at interfacial regions will be investigated using a variety of calculation approaches. These several approaches will provide fundamental information concerning the possible modulation of protein and macromolecule structure by solvent, and provide necessary background information for interpretation of measurements made on more complex systems such as whole tissues.